Ten construction workers will often get a job done faster than one. But in digging a deep well, for instance, ten workers are a waste of human resources: the diggers can’t work simultaneously, as the second worker isn’t able to start digging until the first one has finished, and so on.
A similar challenge is encountered by scientists who study the structure and dynamics of molecules using nuclear magnetic resonance (NMR) spectroscopy. This technique serves as an essential tool in understanding numerous molecules – including proteins, nucleic acids and active pharmaceuticals – in their natural surroundings. It does this by exposing them to electromagnetic radiation and studying the dispersion patterns of the electromagnetic waves that hit the molecules. However, to obtain a full NMR picture of such complex molecules one needs to perform numerous measurements that are based on the same “serial” principle as well digging: hundreds or thousands of one-dimensional scans need to be performed one after the other; these scans need then to be combined to create a unified multidimensional picture of the molecule. While a single scan may take a fraction of a second, multidimensional procedures may last several hours or even days.
A team led by Prof. Lucio Frydman of the Weizmann Institute’s Chemical Physics Department has now found a way to perform multidimensional NMR with a single scan. The new method, described in the December 2002 issue of the Proceedings of the National Academy of Sciences USA (PNAS), is expected to significantly speed up molecular studies routinely performed in diverse fields.
Alex Smith | EurekAlert!
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Researchers from TU Graz and their industry partners have unveiled a world first: the prototype of a robot-controlled, high-speed combined charging system (CCS) for electric vehicles that enables series charging of cars in various parking positions.
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
Actin is the most abundant protein in highly developed cells and has diverse functions in processes like cell stabilization, cell division and muscle...
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